Collect. Czech. Chem. Commun. 1981, 46, 1466-1473

Covalent attachment of chymotrypsin to poly[N-(2-hydroxypropyl)methacrylamide]

Ants Läänea, Vladimír Chytrýb, Mati Hagaa, Peeter Sikka, Aavo Aaviksaara and Jindřich Kopečekb

a Institute of Chemical Physics and Biophysics, Estonian Academy of Sciences, Tallinn 200 001, U.S.S.R.
b Institute of Macromolecular Chemistry, Czechoslovak Academy of Sciences, 162 06 Prague 6, Czechoslovakia


Chymotrypsin has been covalently bound on a water-soluble biocompatible carrier poly[N-(2-hydroxypropyl)methacrylamide] by three different methods. The catalytic activity of the polymer bound enzyme in the reaction with low-molecular substrates coincided with the activity of native chymotrypsin. The protective effect of the carrier polymer in chymotrypsin thermoinactivation at pH 8.0 was larger than at pH 6.1, particularly at higher concentrations of the enzyme (at 10-5M), which indicates that the polymer protects chymotrypsin not only against irreversible thermoinactivation but also against autolysis. Significant protective effect of the carrier polymer in the interaction of the polymer bound enzyme with high-molecular soybean trypsin inhibitor has been found.